5VBX

Crystal structure of holo-[acyl-carrier-protein] synthase (AcpS) from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0006633	biological_process	fatty acid biosynthetic process
A	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0005737	cellular_component	cytoplasm
B	0006633	biological_process	fatty acid biosynthetic process
B	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0005737	cellular_component	cytoplasm
C	0006633	biological_process	fatty acid biosynthetic process
C	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue EDO A 201

Chain	Residue
A	LYS86
A	PRO87
A	THR110
A	LEU111
A	HOH335
B	LYS62

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 202

Chain	Residue
A	ARG48
A	GLN45
A	PRO46
A	VAL47

---

site_id	AC3
Number of Residues	5
Details	binding site for residue NA A 203

Chain	Residue
A	GLU12
A	TYR117
C	GLU114
C	ARG115
C	HIS116

---

site_id	AC4
Number of Residues	5
Details	binding site for residue NA A 204

Chain	Residue
A	VAL19
A	SER23
A	GLY24
A	ARG26
A	LEU27

---

site_id	AC5
Number of Residues	5
Details	binding site for residue NA B 201

Chain	Residue
A	GLU114
A	ARG115
A	HIS116
B	GLU12
B	TYR117

---

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO B 202

Chain	Residue
B	LYS86
B	PRO87
B	THR110
B	LEU111
C	LYS62

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO B 203

Chain	Residue
B	PRO87
B	ARG88
B	LEU89
B	MET107
B	HIS108
B	VAL109

---

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO B 204

Chain	Residue
B	GLN45
B	PRO46
B	VAL47
B	ARG48

---

site_id	AC9
Number of Residues	5
Details	binding site for residue NA C 201

Chain	Residue
B	GLU114
B	ARG115
B	HIS116
C	GLU12
C	TYR117

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO C 202

Chain	Residue
C	GLN45
C	PRO46
C	VAL47
C	ARG48

---

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO C 203

Chain	Residue
A	LYS62
C	GLY85
C	PRO87
C	THR110
C	LEU111
C	HOH312

---

site_id	AD3
Number of Residues	1
Details	binding site for residue EDO C 204

Chain	Residue
C	ARG69

---

site_id	AD4
Number of Residues	3
Details	binding site for residue NA C 205

Chain	Residue
C	ARG88
C	LEU89
C	MET107

---

site_id	AD5
Number of Residues	5
Details	binding site for residue NA C 206

Chain	Residue
C	VAL19
C	SER23
C	GLY24
C	ARG26
C	LEU27

---

site_id	AD6
Number of Residues	3
Details	binding site for residue NA C 207

Chain	Residue
C	ASN81
C	NA209
C	HOH307

---

site_id	AD7
Number of Residues	6
Details	binding site for residue NA C 208

Chain	Residue
C	GLU12
C	ILE13
C	ALA14
C	HIS116
C	HOH314
C	HOH328

---

site_id	AD8
Number of Residues	2
Details	binding site for residue NA C 209

Chain	Residue
C	ARG53
C	NA207

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00101

Chain	Residue	Details
A	ASP9
A	GLU58
B	ASP9
B	GLU58
C	ASP9
C	GLU58

---